ID Q7MVN4_PORGI Unreviewed; 908 AA.
AC Q7MVN4;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN Name=ppdK {ECO:0000313|EMBL:AAQ66137.1};
GN OrderedLocusNames=PG_1017 {ECO:0000313|EMBL:AAQ66137.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66137.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66137.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
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DR EMBL; AE015924; AAQ66137.1; -; Genomic_DNA.
DR RefSeq; WP_005874102.1; NC_002950.2.
DR AlphaFoldDB; Q7MVN4; -.
DR STRING; 242619.PG_1017; -.
DR EnsemblBacteria; AAQ66137; AAQ66137; PG_1017.
DR KEGG; pgi:PG_1017; -.
DR PATRIC; fig|242619.8.peg.940; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_10; -.
DR BioCyc; PGIN242619:G1G02-945-MONOMER; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.80.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:AAQ66137.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:AAQ66137.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000588};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..390
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 456..537
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 553..902
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 489
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 864
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 595
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 651
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 778
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 778
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 799
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 800
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 801
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 802
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 802
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 908 AA; 100485 MW; 1DDFC7339BC89409 CRC64;
MEKKRVYTFG NGKAEGEAGM KNLLGGKGAN LAEMNLIGVP VPPGFTITTE VCQEYYTLGR
DKVVELLRGE VNDAIRNIEG LMKSKFGDTE NPLLVSVRSG ARASMPGMMD TILNLGLNDE
VVAGIVRKTG NERFAWDSYR RFVQMYGDVV LGMKPTNKED IDPFEEIIEK VKEENGVHLD
NELSVENLKD LVSRFKAAVK AQTGKDFPFS AEEQLWGAIM AVFDSWMNER AILYRRMEGI
PAEWGTAVNV QAMVFGNMGE TSATGVCFSR DAGSGEDLFN GEYLINAQGE DVVAGIRTPQ
QITKIGSQRW AERAGIAEDV RVAQYPSMEE AMPEIYKELD TLQQKLEDHY RDMQDMEFTV
QEGKLWFLQT RNGKRTGCAM VKIAMDLLRQ GMISEEEALM RVEPNKLDEL LHPIFDKSAL
LRARVLTKGL PASPGAATGQ IVFFADDAAQ WKEDGKRVVM VRIETSPEDL AGMSAAEGIL
TARGGMTSHA AVVARGMGKC CVSGAGALNI DYKARTVEID GTLFKEGDYI SINGSTGEIY
EGQVETKAAE MDQDFADLMA LADKYAKLKV RTNADTPHDA EIARSFGAVG IGLCRTEHMF
FEGEKIKAMR EMILSETAEG RVRALAKILP YQQEDFKGIF RAMNGFPVNV RLLDPPLHEF
VPHDLKGQEE MARMMGVDVR IIQKRVEDLM EHNPMLGHRG CRLGNTYPEI TEMQTRAILG
ACLELKKEGV VCLPEIMVPL TGILHEFKHQ EEVIRATAAK LFEEKGDSVE FQVGTMIEVP
RAALTADRIA SSAEFFSFGT NDLTQMTFGY SRDDIASFLP IYLDKKILKV DPFQVLDQKG
VGQLVRMATE NGRKARPNLK CGICGEHGGE PSSVKFCHRV GLNYVSCSPF RVPIARLAAA
QAVIEEGK
//
